Sumit Kumar Chaturvedi

ORCID: 0000-0003-3600-8883
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About
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Research Areas
  • Protein Interaction Studies and Fluorescence Analysis
  • Protein Structure and Dynamics
  • Alzheimer's disease research and treatments
  • Protein purification and stability
  • Drug Transport and Resistance Mechanisms
  • Surfactants and Colloidal Systems
  • Digital Marketing and Social Media
  • Technology Adoption and User Behaviour
  • Enzyme Structure and Function
  • Computational Drug Discovery Methods
  • Monoclonal and Polyclonal Antibodies Research
  • RNA Research and Splicing
  • Cholinesterase and Neurodegenerative Diseases
  • Data Visualization and Analytics
  • Photosynthetic Processes and Mechanisms
  • Spectroscopy and Quantum Chemical Studies
  • Microtubule and mitosis dynamics
  • DNA and Nucleic Acid Chemistry
  • 14-3-3 protein interactions
  • Viral Infectious Diseases and Gene Expression in Insects
  • Bacteriophages and microbial interactions
  • Glycosylation and Glycoproteins Research
  • Prion Diseases and Protein Misfolding
  • Microfluidic and Bio-sensing Technologies
  • Heat shock proteins research

National Institute of Biomedical Imaging and Bioengineering
2017-2024

National Institutes of Health
2017-2024

University of Delhi
2023-2024

Washington University in St. Louis
2023

Indian Institute of Soil and Water Conservation
2021

Aligarh Muslim University
2011-2020

JECRC University
2014-2017

Jaipuria Institute of Management
2014-2016

Advanced Micro Devices (United States)
2012

Old Dominion University
1994-2005

Mechanistic insight into the BSA–limonene interaction: biophysical and molecular docking approach.

10.1039/c4mb00548a article EN Molecular BioSystems 2014-10-23

Abstract Protein misfolding and aggregation have been associated with several human diseases such as Alzheimer’s, Parkinson’s familial amyloid polyneuropathy etc. In this study, anti-fibrillation activity of vitamin k3 its effect on the kinetics formation hen egg white lysozyme (HEWL) Aβ-42 peptide were investigated. Here, in combination Thioflavin T (ThT) fluorescence assay, circular dichroism (CD), transmission electron microscopy cell cytotoxicity we demonstrated that significantly...

10.1038/srep26759 article EN cc-by Scientific Reports 2016-05-27

Sodium dodecyl sulphate (SDS), an anionic surfactant that mimics some characteristics of biological membrane has also been found to induce aggregation in proteins. The present study was carried out on 25 diverse proteins using circular dichroism, fluorescence spectroscopy, dye binding assay and electron microscopy. It appropriate molar ratio protein SDS readily induced amyloid formation all at a pH below two units their respective isoelectric points (pI) while no observed above pI. We...

10.1371/journal.pone.0029694 article EN cc-by PLoS ONE 2012-01-12

Different proteins have different amino acid sequences as well conformations, and therefore propensities to aggregate. Electrostatic interactions an important role in the aggregation of revealed by our previous report (J. M. Khan et al., PLoS One, 2012, 7, e29694). In this study, we designed executed experiments gain knowledge charge variations on during events protein with lysozyme a model protein. To impart positive negative charges proteins, incubated at pH values below above pI (∼11)....

10.1039/c3sm52435c article EN Soft Matter 2014-01-01

Amyloid fibril formation by proteins leads to variety of degenerative disorders called amyloidosis. While these are topic extensive research, effective treatments still unavailable. Thus in present study, two anti-tuberculosis drugs, i.e., pyrazinamide (PYZ) and D-cycloserine (DCS), also known for treatment Alzheimer's dementia, were checked the anti-aggregation anti-amyloidogenic ability on Aβ-42 peptide hen egg white lysozyme. Results demonstrated that both drugs inhibit heat induced...

10.1371/journal.pone.0136528 article EN cc-by PLoS ONE 2015-08-27

In concentrated macromolecular solutions, weak physical interactions control the solution behavior including particle size distribution, aggregation, liquid-liquid phase separation, or crystallization. This is central to many fields ranging from colloid chemistry cell biology and pharmaceutical protein engineering. Unfortunately, it very difficult determine assembly states polydispersity at high concentrations in solution, since all motion coupled through long-range hydrodynamic,...

10.1038/s41467-018-06902-x article EN cc-by Nature Communications 2018-10-18

Banana lectin (BL) is a homodimeric protein categorized among jacalin-related family of lectins. The effect acidic pH was examined on conformational stability BL by using circular dichroism, intrinsic fluorescence, 1-anilino-8-napthalene sulfonate (ANS) binding, size exclusion chromatography (SEC) and dynamic light scattering (DLS). During acid denaturation BL, the monomerization native dimeric found at 2.0. elution profile from SEC showed two different peaks (59.65 ml & 87.98 ml) 2.0 while...

10.1371/journal.pone.0062428 article EN cc-by PLoS ONE 2013-04-26

The present study details the binding process of clofazimine to hen egg white lysozyme (HEWL) using spectroscopy, dynamic light scattering, transmission electron microscopy (TEM), and molecular docking techniques. Clofazimine binds protein with constant (Kb) in order 1.57 × 104 at 298 K. Binding is spontaneous exothermic. Molecular results suggested involvement hydrogen bonding hydrophobic interactions process. Bacterial cell lytic activity presence increased more than 40% value obtained...

10.1080/07391102.2016.1211552 article EN Journal of Biomolecular Structure and Dynamics 2016-07-11

We introduce SynthLight, a diffusion model for portrait relighting. Our approach frames image relighting as re-rendering problem, where pixels are transformed in response to changes environmental lighting conditions. Using physically-based rendering engine, we synthesize dataset simulate this lighting-conditioned transformation with 3D head assets under varying lighting. propose two training and inference strategies bridge the gap between synthetic real domains: (1) multi-task that takes...

10.48550/arxiv.2501.09756 preprint EN arXiv (Cornell University) 2025-01-16

Negatively charged species such as nucleic acids have commonly been found to be associated with the proteinaceous deposits in tissues of patients amyloid diseases.

10.1039/c6ra01079b article EN RSC Advances 2016-01-01

Abstract Amyloid fibrillation is associated with several human maladies, such as Alzheimer’s, Parkinson’s, Huntington’s diseases, prions, amyotrophic lateral sclerosis, and type 2 diabetes diseases. Gaining insights into the mechanism of amyloid fibril formation exploring novel approaches to inhibition are crucial for preventing Here, we hypothesized that ligands capable stabilizing native state query proteins might prevent protein unfolding, which, in turn, may reduce propensity form...

10.1002/jcb.27576 article EN Journal of Cellular Biochemistry 2018-09-22
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